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Crystal structure of B. pseudomallei fabi in complex with NAD and triclosan

Analyse Crystal structure of B. pseudomallei fabi in complex with NAD and triclosan in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IFL
Type: protein
Length: 4,080 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-[acyl-carrier-protein] reductase [NADH]
EC: 1.3.1.9
UniProt: A0A069B9A4
Ligands: TCL, NAD
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	255	47% helix, 17% strand	A0A069B9A4

Ligands and binding sites

TCL · Triclosan · ligand · 16 copies · chains B, A, C, D, E, F, G, H, I, J, K, L, M, N, O, P
NAD · Nicotinamide-adenine-dinucleotide · ligand · 16 copies · chains B, A, C, D, E, F, G, H, I, J, K, L, M, N, O, P

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1131	0.85	0.86	51	empty
2	1137	0.84	0.86	55	empty
3	1132	0.84	0.85	53	empty
4	1170	0.84	0.85	55	empty
5	716	0.83	0.86	54	TCL, NAD

Interfaces

31 interfaces between chains.

M–N · 1663 Å² buried · 35 hydrogen bonds · protein-protein
B–A · 1656 Å² buried · 30 hydrogen bonds · protein-protein
K–L · 1654 Å² buried · 32 hydrogen bonds · protein-protein
E–F · 1649 Å² buried · 34 hydrogen bonds · protein-protein
C–D · 1645 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

5IFL · Crystal structure of B. pseudomallei FabI in complex with NAD and triclosan · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A069B9A4
Elsewhere: RCSB PDB 5IFL · PDBe 5IFL · UniProt A0A069B9A4

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